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Reviewed, UniProtKB/Swiss-Prot Q64520 (KGUA_MOUSE)

Last modified November 24, 2009. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Guanylate kinase
    EC=2.7.4.8
Alternative name(s):
    GMP kinase
Gene names
Name: Guk1
Synonyms: Gmk
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length198 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Essential for recycling GMP and indirectly, cGMP.

Catalytic activity

ATP + GMP = ADP + GDP.

Subunit structure

Monomer By similarity.

Sequence similarities

Belongs to the guanylate kinase family.

Contains 1 guanylate kinase-like domain.

Ontologies

Keywords
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Gene Ontology (GO)
   Biological processpurine nucleotide metabolic process Ref.1

Inferred from direct assay. Source: UniProtKB

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

guanylate kinase activity Ref.1

Inferred from direct assay. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 198197Guanylate kinase
PRO_0000170652

Regions

Domain4 – 186183Guanylate kinase-like
Nucleotide binding11 – 188ATP By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue531Phosphotyrosine Ref.3

Secondary structure

................................... 198
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q64520-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: F584E4B6521C607B

FASTA19821,918
        10         20         30         40         50         60 
MAGPRPVVLS GPSGAGKSTL LKKLFQEHSS IFGFSVSHTT RNPRPGEEDG KDYYFVTREM 

        70         80         90        100        110        120 
MQRDIAAGDF IEHAEFSGNL YGTSKEAVRA VQAMNRICVL DVDLQGVRSI KKTDLCPIYI 

       130        140        150        160        170        180 
FVQPPSLDVL EQRLRLRNTE TEESLAKRLA AARTDMESSK EPGLFDLVII NDDLDKAYAT 

       190 
LKQALSEEIK KAQGTGHA 

« Hide

References

« Hide 'large scale' references
[1]"Cloning, characterization, and modeling of mouse and human guanylate kinases."
Brady W.A., Kokoris M.S., Fitzgibbon M., Black M.E.
J. Biol. Chem. 271:16734-16740(1996) [PubMed: 8663313] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Mammary gland.
[3]"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
J. Proteome Res. 7:311-318(2008) [PubMed: 18034455] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-53, MASS SPECTROMETRY.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

U53514 mRNA. Translation: AAC52652.1.
BC024625 mRNA. Translation: AAH24625.1.
IPIIPI00929789.
UniGeneMm.3624

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1LVGX-ray2.10A1-198[»]
ModBaseSearch...

Protein-protein interaction databases

STRINGQ64520.

PTM databases

PhosphoSiteQ64520.

Proteomic databases

PRIDEQ64520.

Genome annotation databases

EnsemblENSMUST00000102702; ENSMUSP00000099763; ENSMUSG00000020444; Mus musculus. [Genome view]
NMPDRfig|10090.3.peg.23792.
UCSCuc007jdg.1. mouse.

Organism-specific databases

MGIMGI:95871. Guk1.

Phylogenomic databases

HOVERGENQ64520.
OrthoDBEOG9323HS

Enzyme and pathway databases

BRENDA2.7.4.8. 244.

Gene expression databases

ArrayExpressQ64520.
BgeeQ64520.
CleanExMM_GUK1.
GenevestigatorQ64520.
GermOnlineENSMUSG00000020444. Mus musculus.

Family and domain databases

InterProIPR008144. Guanylate_kin.
IPR020590. Guanylate_kinase_CS.
IPR017665. Guanylate_kinase_sub.
IPR008145. Guanylt/Ca.
[Graphical view]
PfamPF00625. Guanylate_kin. 1 hit.
[Graphical view]
SMARTSM00072. GuKc. 1 hit.
[Graphical view]
TIGRFAMsTIGR03263. guanyl_kin. 1 hit.
PROSITEPS00856. GUANYLATE_KINASE_1. 1 hit.
PS50052. GUANYLATE_KINASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio287231.
SOURCESearch...

Entry information

Entry nameKGUA_MOUSE
AccessionPrimary (citable) accession number: Q64520
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: November 24, 2009
This is version 78 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents